Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 359460
Title On the mechanism of uptake of globular proteins by polyelectrolyte brushes: A two gradient self-consistent field analysis
Author(s) Leermakers, F.A.M.; Ballauff, M.; Borisov, O.V.
Source Langmuir 23 (2007)7. - ISSN 0743-7463 - p. 3937 - 3946.
DOI https://doi.org/10.1021/la0632777
Department(s) Physical Chemistry and Colloid Science
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) aqueous-solution - polymer brushes - adsorption - layer - model - binding
Abstract We present model calculations for the interaction of a protein-like inhomogeneously charged nanoscale object with a layer of densely grafted polyelectrolytes ("polyelectrolyte brush"). The motivation of this work is the recent experimental observation that proteins that carry an overall negative charge are absorbed into negatively charged polyelectrolyte brushes. Two-gradient self-consistent field (2G-SCF) calculations have been performed to unravel the physical mechanism of the uptake of protein thus effected. Our results prove that an overall neutral, protein-like object can electrostatically be attracted and therefore spontaneously driven into a polyelectrolyte brush when the object has two faces (patches, domains), one with a permanent positive charge and the other with a permanent negative charge. Using a 2G-SCF analysis, we evaluate the free energy of insertion, such that the electric dipole of the inclusion is oriented parallel to the brush surface. An electroneutral protein-like object is attracted into the brush because the polyelectrolyte brush interacts asymmetrically with the charged patches of opposite sign. At high ionic strength and low charge density on the patches, the attraction cannot compete with the repulsive excluded-volume interaction. However, for low ionic strengths and sufficiently high charge density on the patches, a gain on the order of kBT per charge becomes possible. Hence, the asymmetry of interaction for patches of different charges may result in a total attractive force between the protein and the brush. All results obtained herein are in excellent agreement with recent experimental data.
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